ID   CESSA_CONBY             Reviewed;         121 AA.
AC   P0DTJ2;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Conopressin-conophysin {ECO:0000305};
DE   Contains:
DE     RecName: Full=Conopressin-ba1a {ECO:0000303|PubMed:33916793};
DE     AltName: Full=Conopressin-ba1c {ECO:0000303|PubMed:33916793};
DE   Contains:
DE     RecName: Full=Conopressin-ba1b {ECO:0000303|PubMed:33916793};
DE   Contains:
DE     RecName: Full=Conophysin ba1 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus bayani (Bayan's cone) (Stellaconus bayani).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Splinoconus.
OX   NCBI_TaxID=2070216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-30, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AMIDATION AT GLY-29, AND HYDROXYLATION AT PRO-27.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=33916793; DOI=10.3390/md19040202;
RA   Rajaian Pushpabai R., Wilson Alphonse C.R., Mani R., Arun Apte D.,
RA   Franklin J.B.;
RT   "Diversity of Conopeptides and Conoenzymes from the Venom Duct of the
RT   Marine Cone Snail Conus bayani as Determined from Transcriptomic and
RT   Proteomic Analyses.";
RL   Mar. Drugs 19:0-0(2021).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33916793}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:33916793}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: [Conopressin-ba1b]: Mass=1081.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:33916793};
CC   -!- MASS SPECTROMETRY: [Conopressin-ba1a]: Mass=1023.5; Method=MALDI;
CC       Note=amidated, not hydroxylated.;
CC       Evidence={ECO:0000269|PubMed:33916793};
CC   -!- MASS SPECTROMETRY: Mass=1039.5; Method=MALDI; Note=Conopressin-ba1c,
CC       amidated, hydroxylated.; Evidence={ECO:0000269|PubMed:33916793};
CC   -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005185; F:neurohypophyseal hormone activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.9.10; -; 1.
DR   InterPro; IPR000981; Neurhyp_horm.
DR   InterPro; IPR036387; Neurhyp_horm_dom_sf.
DR   InterPro; IPR022423; Neurohypophysial_hormone_CS.
DR   PANTHER; PTHR11681; PTHR11681; 1.
DR   Pfam; PF00220; Hormone_4; 1.
DR   Pfam; PF00184; Hormone_5; 1.
DR   PRINTS; PR00831; NEUROPHYSIN.
DR   SMART; SM00003; NH; 1.
DR   SUPFAM; SSF49606; SSF49606; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000305|PubMed:33916793"
FT   PEPTIDE         21..30
FT                   /note="Conopressin-ba1b"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT                   /id="PRO_0000454976"
FT   PEPTIDE         21..29
FT                   /note="Conopressin-ba1a"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT                   /id="PRO_0000454977"
FT   CHAIN           33..121
FT                   /note="Conophysin ba1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A4Y5X1A7"
FT                   /id="PRO_0000454978"
FT   MOD_RES         27
FT                   /note="4-hydroxyproline; partial; in Conopressin-ba1c"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT   MOD_RES         29
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:33916793"
FT   DISULFID        21..26
FT                   /evidence="ECO:0000250|UniProtKB:P05486"
FT   DISULFID        43..83
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        51..73
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        90..108
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        102..120
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
FT   DISULFID        109..114
FT                   /evidence="ECO:0000250|UniProtKB:P01175"
SQ   SEQUENCE   121 AA;  12861 MW;  30399AF0AF305403 CRC64;
     MGRLTMALCW LLLLLLTTQA CYITNCPRGG KRDVDDGLGV RPCMFCSFGQ CVGPHICCGA
     GGCEIGTLEA STCHEENENP IPCHVFGDRC LLKHPGNVHG NCVSPGVCCT DDTCSMHVGC
     L